Purification and biochemical characterization of a mouse submandibular sialomucin.
A sialomucin from the mouse submandibular gland was isolated and purified by a protocol involving Sephacryl S-200 chromatography, acidic dialysis, and preparative, poly(acrylamide)-gel electrophoresis. The mucus glycoprotein was judged to be free from contaminants by analytical and sodium dodecyl sulfate-poly(acrylamide)-gel electrophoresis, isoelectric focusing, immunoelectrophoresis, and immunodiffusion when made visible by Stains-all, periodic acid-Schiff reagent, and Coomassie Blue. The carbohydrate portion constituted 81% of the weight of the mucus glycoprotein, and was composed of 2-acetamido-2-deoxy-D-glucose, 2-acetamido-2-deoxy-D-galactose, sialic acid, D-galactose, and D-mannose. Neither L-fucose nor sulfate was detected. The aliphatic amino acids constituted 60% of the protein core. The sialomucin has an apparent mol. wt. of 140,000 by sodium dodecyl sulfate-gel electrophoresis, and a pI of 2.77-3.63 by isoelectric focusing.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D005260:Female; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D051379:Mice; D008970:Molecular Weight; D009077:Mucins / Q000302:isolation & purification*; D012795:Sialoglycoproteins / Q000302:isolation & purification*; D052116:Sialomucins; D013363:Submandibular Gland / Q000032:analysis*
D000596:Amino Acids; D002241:Carbohydrates; D009077:Mucins; D012795:Sialoglycoproteins; D052116:Sialomucins